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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

impdh

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K+UniRule annotation

Enzyme regulationi

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (impdh)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi329Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi331Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei332IMPUniRule annotation1
Active sitei334Thioimidate intermediateUniRule annotation1
Metal bindingi334Potassium; via carbonyl oxygenUniRule annotation1
Active sitei430Proton acceptorUniRule annotation1
Binding sitei442IMPUniRule annotation1
Metal bindingi501Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi502Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi277 – 279NADUniRule annotation3
Nucleotide bindingi327 – 329NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

ReactomeiR-DDI-6798695. Neutrophil degranulation.
R-DDI-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Gene namesi
Name:impdh
Synonyms:guaB
ORF Names:DDB_G0283701
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0283701. guaB.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: dictyBase
  • phagocytic vesicle Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003281521 – 515Inosine-5'-monophosphate dehydrogenaseAdd BLAST515

Proteomic databases

PaxDbiQ54QQ0.

Expressioni

Inductioni

Down-regulated by Legionella pneumophila infection.1 Publication

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi44689.DDB0230098.

Structurei

3D structure databases

ProteinModelPortaliQ54QQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini120 – 179CBS 1UniRule annotationAdd BLAST60
Domaini183 – 239CBS 2UniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 369IMP bindingUniRule annotation3
Regioni390 – 391IMP bindingUniRule annotation2
Regioni414 – 418IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
InParanoidiQ54QQ0.
KOiK00088.
OMAiKWMVGAA.
PhylomeDBiQ54QQ0.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q54QQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKINKILQG TNSEYKSEWF VDGFDCFELF QQRHGYTYDD LIMLPGHINF
60 70 80 90 100
SADDVSLKTK LTKNISLNAP LVSSPMDTVT EHLMAINMAL LGGIGIIHYN
110 120 130 140 150
NTVEEQVVEV KKVKRFKNGF ITDPIVLSPT HKLSDVDMIK QKYGFSGIPI
160 170 180 190 200
TDTGRIGGKL VGIVTSRDTD FIKDRSTTLS EVMTTDLITG QQNCTLEEAN
210 220 230 240 250
SILKSCKKGK LPIVNDKGEL VALASRDDLV KNRDFPMATK DHENKKLLVG
260 270 280 290 300
AALGTRETDK ERLAALSDAG VDVVILDSSQ GDSTYQREMI RFIKRNYPKI
310 320 330 340 350
DVIGGNVVTT SQCESLIQAG VDGLRVGMGV GSICTTQEVM ACGRPQATAV
360 370 380 390 400
FKCALYSSQY NVPIIADGGI RTIGHIIKGL SLGASSVMMG SMLAGTEEAP
410 420 430 440 450
GDYFYKDGMR LKKYRGMGSL EAMVKGGDQR YFSETDKIKV AQGVSGSVVD
460 470 480 490 500
KGSVKKFVPY LIQGIKHGLQ DLGCNSVTNL RESVYGGKVR FEVRTAAAQV
510
EGSVHSLFSY EKHFI
Length:515
Mass (Da):56,311
Last modified:May 24, 2005 - v1
Checksum:i054EFBD2EB940868
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000056 Genomic DNA. Translation: EAL65617.1.
RefSeqiXP_638973.1. XM_633881.1.

Genome annotation databases

EnsemblProtistsiEAL65617; EAL65617; DDB_G0283701.
GeneIDi8624219.
KEGGiddi:DDB_G0283701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000056 Genomic DNA. Translation: EAL65617.1.
RefSeqiXP_638973.1. XM_633881.1.

3D structure databases

ProteinModelPortaliQ54QQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0230098.

Proteomic databases

PaxDbiQ54QQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL65617; EAL65617; DDB_G0283701.
GeneIDi8624219.
KEGGiddi:DDB_G0283701.

Organism-specific databases

dictyBaseiDDB_G0283701. guaB.

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
COG0517. LUCA.
InParanoidiQ54QQ0.
KOiK00088.
OMAiKWMVGAA.
PhylomeDBiQ54QQ0.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
ReactomeiR-DDI-6798695. Neutrophil degranulation.
R-DDI-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiQ54QQ0.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIMDH_DICDI
AccessioniPrimary (citable) accession number: Q54QQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: November 30, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.